Protein components of quenched adhesive secretaons formed by the sea mussel, Mytilus edulis, will be separated, isolated, and purified and characterized biochemically and biophysically. Adhesive secretions will be collected in the presence of sodium cyanide to present adhesive setting. Proteins in the quenched-adhesive substance will be separated by gel permeation and ion-exchange chromatography. Protein fractions will be subsequently analyzed for biochemical and biophysical properties. Continued fractionation of isolated proteins will be initiated in efforts to identify peptides and/or amino acid residues directly involved in adhesive hardening mechanisms.